E. coli bacterioferritin was crystallized in a novel crystal form from different conditions and the structure was solved. The crystals belonged to space group P213 and diffracted to a resolution of 2.5 Å.

The structure of UDP-3-O-acyl-N-acetylglucosamine deacetylase (LpxC) in complex with UDP is reported. The complex allows for a description of how the enzyme recognizes and binds a nucleotide moiety and enables the construction of an LpxC-substrate model.

The crystallization of GADPH from S. oleracea in two different space groups has been accomplished using GAPDH samples with unusually low purity levels. One crystal form is the same as a previously reported form, while the second represents a new form. The quality of the diffraction allowed the structure to be determined at a 3 Å resolution limit.

The crystallization and preliminary X-­ray data of Canavalia gladiata lectin (CGL) and C. maritima lectin (CML) complexed with Man(α1-2)Man(α1)OMe, Man(α1-3)Man(α1)OMe and Man(α1-4)Man(α1)OMe in two crystal forms [the complexes with Man(α1-3)Man(α1)OMe and Man(α1-4)Man(α1)OMe crystallized in space group P32 and those with Man(α1-2)Man(α1)OMe crystallized in space group I222], which differed from those of the native proteins (P21212 for CML and C222 for CGL), are reported.

α-11 giardin from the intestinal protozoan parasite, G. lamblia has been cloned, expressed, purified and crystallized under two different conditions and in two different space groups. Crystals from the first condition diffracted to 1.1 Å and belong to a primitive orthorhombic space group and crystals obtained in the second condition diffracted to 2.93 Å and belong to a primitive monoclinic space group.

M. tuberculosis dihydrodipicolinate synthase, the enzyme that catalyzes the first unique reaction in the L-lysine biosynthesis pathway, has been cloned, expressed, purified and crystallized and the crystals have been characterized by X-ray diffraction.

Human recombinant tumour suppressor S100A2 and a mutant lacking cysteine residues have been purified and crystallized. Only the crystals of the mutant protein diffracted to appropriate resolution and a complete data set was recorded at 1.7 Å.

The Corynebacterium glutamicum NTA monooxygenase component A protein, which plays the central role in NTA biodegradation, was crystallized. The initial X-ray crystallographic characterization is reported.

Human S100A13 protein was cloned, expressed, purified and crystallized by the hanging-drop vapour-diffusion method. The crystals obtained belonged to space group P212121 and diffracted to a resolution of 1.8 Å.

An aromatic prenyltransferase (CloQ) from S. roseochromogenes that is implicated in clorobiocin biosynthesis has been crystallized in space group I4122. X-ray data to 2.2 Å resolution were collected in-house.

The crystallization and data collection of topoisomerase IV from S. aureus is described. Phasing by molecular replacement proved difficult owing to the presence of translational NCS and strategies used to overcome this are discussed.